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Results 1 - 4 of 4
EC Number Cofactor Commentary Reference
Display the reaction diagram Show all sequences 1.14.15.36cytochrome P450 the oxidized absolute spectrum of the purified CYP51, in the absence of substrate, shows a Soret band at 417 nm and alpha-, beta-, and delta-bands at 569, 535, and 369 nm 749797
Display the reaction diagram Show all sequences 1.14.15.36cytochrome P450 the oxidized absolute spectrum of the purified enzyme, in the absence of substrate, shows a Soret band at 417 nm and alpha-,beta-, and delta bands at 569, 535, and 369 nm 752067
Display the reaction diagram Show all sequences 1.14.15.36Ferredoxin - 749882
Display the reaction diagram Show all sequences 1.14.15.36heme heme-iron reduction is the rate limiting step in catalysis. Protonation of the cysteinate ligand to the ferrous CYP51 underlies the collapse of the Fe(II)-CO adduct of the enzyme from its P450 to its P420 form. The protonation is reversible and the rate of P420 formation is substantially retarded in the estriol-bound form of CYP51 749882
Results 1 - 4 of 4